REGULATION OF LETHOCERUS INSECT FLIGHT MUSCLES

花荽昆虫飞行肌肉的调节

• 批准号: 3779595
• 负责人: F WANG
• 金额: --
• 依托单位: NATIONAL HEART, LUNG, AND BLOOD INSTITUTE
• 依托单位国家: 美国
• 资助国家: 美国
• 起止时间: 至
• 项目状态: 未结题
• 来源: https://reporter.nih.gov/project-details/3779595
• 关键词: SDS polyacrylamide gel electrophoresis; actins; alternatives to animals in research; calcium; enzyme activity; muscle contraction; myofibrils; myosin light chain kinase; myosins; phosphorylation; protein purification; protein sequence; striated muscles

The insect flight muscle (IFM) of Lethocerus has an almost crystalline sarcomere structure and has been the subject of many ultrastructural investigations. Considerably less is known about the biochemical function and regulation of the individual contractile proteins from this muscle. We have purified myosin from IFM of Lethocerus and have studied its ability to translocate actin filaments in an in vitro motility assay. Since some invertebrate myosins are regulated by direct calcium binding to the myosin and others by phosphorylation of the regulatory light chain subunit of myosin, we have tried to study what role the phosphorylation may play in insect flight muscle. Lethocerus myosin from different preparations shows three to four light chains on SDS-PAGE, two to three of which can be phosphorylated either by smooth muscle myosin light chain kinase or by an endogenous myosin light chain kinase. The role of phosphorylation is still unclear at the present time.

Lethocerus的昆虫飞行肌（IFM）几乎是结晶状的。 肌节结构，并已成为许多超微结构的主题 调查事务所 我们对生物化学的了解少得多， 从这一点上，单个收缩蛋白的功能和调节 肌肉. 我们从Lethocerus的IFM中纯化了肌球蛋白， 其在体外运动性测定中移位肌动蛋白丝的能力。 由于一些无脊椎动物肌球蛋白是由直接钙结合调节 通过调节轻链的磷酸化作用， 肌球蛋白亚基，我们试图研究磷酸化的作用， 可能在昆虫的飞行肌肉中起作用。 白蛉肌球蛋白来自不同的 制备物在SDS-PAGE上显示三至四条轻链，两至三条轻链， 其中的一种可以被平滑肌肌球蛋白轻链磷酸化， 激酶或内源性肌球蛋白轻链激酶。 的作用 磷酸化目前仍不清楚。